ID DAD1_YEAST Reviewed; 94 AA. AC Q12248; D6VS02; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 07-OCT-2020, entry version 148. DE RecName: Full=DASH complex subunit DAD1; DE AltName: Full=DUO1 and DAM1-interacting protein 1; DE AltName: Full=Outer kinetochore protein DAD1; GN Name=DAD1; OrderedLocusNames=YDR016C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [4] RP COMPONENT OF DASH COMPLEX. RX PubMed=11799062; DOI=10.1101/gad.959402; RA Li Y., Bachant J.B., Alcasabas A.A., Wang Y., Qin J., Elledge S.J.; RT "The mitotic spindle is required for loading of the DASH complex onto the RT kinetochore."; RL Genes Dev. 16:183-197(2002). RN [5] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP FUNCTION. RX PubMed=15664196; DOI=10.1016/j.molcel.2004.12.019; RA Westermann S., Avila-Sakar A., Wang H.-W., Niederstrasser H., Wong J., RA Drubin D.G., Nogales E., Barnes G.; RT "Formation of a dynamic kinetochore-microtubule interface through assembly RT of the Dam1 ring complex."; RL Mol. Cell 17:277-290(2005). RN [8] RP FUNCTION. RX PubMed=16415853; DOI=10.1038/nature04409; RA Westermann S., Wang H.-W., Avila-Sakar A., Drubin D.G., Nogales E., RA Barnes G.; RT "The Dam1 kinetochore ring complex moves processively on depolymerizing RT microtubule ends."; RL Nature 440:565-569(2006). RN [9] RP SUBUNIT. RX PubMed=16715078; DOI=10.1038/ncb1414; RA Joglekar A.P., Bouck D.C., Molk J.N., Bloom K.S., Salmon E.D.; RT "Molecular architecture of a kinetochore-microtubule attachment site."; RL Nat. Cell Biol. 8:581-585(2006). RN [10] RP FUNCTION. RX PubMed=16777964; DOI=10.1073/pnas.0602249103; RA Asbury C.L., Gestaut D.R., Powers A.F., Franck A.D., Davis T.N.; RT "The Dam1 kinetochore complex harnesses microtubule dynamics to produce RT force and movement."; RL Proc. Natl. Acad. Sci. U.S.A. 103:9873-9878(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [13] RP ELECTRON MICROSCOPY OF DASH COMPLEX ALONE AND BOUND TO MICROTUBULES. RX PubMed=15640796; DOI=10.1038/nsmb896; RA Miranda J.L., Wulf P.D., Sorger P.K., Harrison S.C.; RT "The yeast DASH complex forms closed rings on microtubules."; RL Nat. Struct. Mol. Biol. 12:138-143(2005). CC -!- FUNCTION: Component of the DASH complex, a microtubule-binding CC subcomplex of the outer kinetochore that is essential for proper CC chromosome segregation. The DASH complex mediates the formation and CC maintenance of bipolar kinetochore-microtubule attachments by forming CC closed rings around spindle microtubules and establishing interactions CC with proteins from the central kinetochore. The DASH ring complex may CC both stabilize microtubules during chromosome attachment in anaphase A, CC and allow the chromosome to remain attached to the depolymerizing CC microtubule in anaphase B. Microtubule depolymerization proceeds by CC protofilament splaying and induces the kinetochore-attached ring to CC slide longitudinally, thereby helping to transduce depolymerization CC energy into pulling forces to disjoin chromatids. CC {ECO:0000269|PubMed:15664196, ECO:0000269|PubMed:16415853, CC ECO:0000269|PubMed:16777964}. CC -!- SUBUNIT: The DASH complex is an approximately 210 kDa heterodecamer, CC which consists of ASK1, DAD1, DAD2, DAD3, DAD4, DAM1, DUO1, HSK3, SPC19 CC and SPC34, with an apparent stoichiometry of one copy of each subunit. CC DASH oligomerizes into a 50 nm ring composed of about 16 molecules that CC encircles the microtubule. Integrity of the complex and interactions CC with central kinetochore proteins are regulated by the spindle assembly CC checkpoint kinase IPL1. {ECO:0000269|PubMed:16715078}. CC -!- INTERACTION: CC Q12248; P53267: DAM1; NbExp=4; IntAct=EBI-35662, EBI-23268; CC Q12248; P53168: DUO1; NbExp=3; IntAct=EBI-35662, EBI-23800; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm, CC cytoskeleton, spindle {ECO:0000269|PubMed:14562095}. Chromosome, CC centromere, kinetochore {ECO:0000269|PubMed:14562095}. Note=Associates CC with the mitotic spindle and the kinetochore. CC -!- MISCELLANEOUS: Present with 799 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the DASH complex DAD1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z74312; CAA98836.1; -; Genomic_DNA. DR EMBL; Z49770; CAA89841.1; -; Genomic_DNA. DR EMBL; AY557635; AAS55961.1; -; Genomic_DNA. DR EMBL; BK006938; DAA11862.1; -; Genomic_DNA. DR PIR; S54639; S54639. DR RefSeq; NP_010299.3; NM_001180324.3. DR SMR; Q12248; -. DR BioGRID; 32066; 355. DR ComplexPortal; CPX-1041; DASH complex. DR DIP; DIP-1296N; -. DR IntAct; Q12248; 9. DR MINT; Q12248; -. DR STRING; 4932.YDR016C; -. DR iPTMnet; Q12248; -. DR MaxQB; Q12248; -. DR PaxDb; Q12248; -. DR PRIDE; Q12248; -. DR EnsemblFungi; YDR016C_mRNA; YDR016C; YDR016C. DR GeneID; 851579; -. DR KEGG; sce:YDR016C; -. DR EuPathDB; FungiDB:YDR016C; -. DR SGD; S000002423; DAD1. DR eggNOG; ENOG502SBWQ; Eukaryota. DR HOGENOM; CLU_142427_2_2_1; -. DR InParanoid; Q12248; -. DR KO; K11553; -. DR PRO; PR:Q12248; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; Q12248; protein. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0042729; C:DASH complex; IDA:SGD. DR GO; GO:0072686; C:mitotic spindle; IEA:InterPro. DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central. DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central. DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:SGD. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007052; P:mitotic spindle organization; IEA:InterPro. DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IDA:SGD. DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:SGD. DR InterPro; IPR013958; DASH_Dad1. DR PANTHER; PTHR28025; PTHR28025; 1. DR Pfam; PF08649; DASH_Dad1; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition; KW Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis; Nucleus; KW Phosphoprotein; Reference proteome. FT CHAIN 1..94 FT /note="DASH complex subunit DAD1" FT /id="PRO_0000127613" FT MOD_RES 91 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18407956" SQ SEQUENCE 94 AA; 10516 MW; 6D27737AC5A39D51 CRC64; MMASTSNDEE KLISTTDKYF IEQRNIVLQE INETMNSILN GLNGLNISLE SSIAVGREFQ SVSDLWKTLY DGLESLSDEA PIDEQPTLSQ SKTK //